Kinetic regime of aggregation of UV-irradiated glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle

The study of the kinetics of aggregation of UV-irradiated proteins has attracted considerable interest, since test systems based on aggregation of proteins denatured by UV radiation can be used for screening of the natural and artificial agents possessing chaperone-like activity (anti-aggregation activity). To provide the proper interpretation of the effects caused by the agents under study, the kinetic mechanism of the aggregation process should be established. In the present work the kinetic data on aggregation of UV-irradiated glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from rabbit skeletal muscle at 37 °C (O.I. Maloletkina et al. Biophys. Chem. 163–164 (2012) 11–20) have been analyzed. It has been shown that the stage of aggregate growth follows the first-order kinetics and the experimentally measured rate constant of the first order corresponds to heat-induced structural reorganization of UV-irradiated GAPDH containing concealed damage. •Kinetic regime of aggregation of UV-irradiated glyceraldehyde-3-phosphate dehydrogenase at 37°C has been established.•The rate of stage of aggregate growth is limited by monomolecular structural reorganization of the irradiated protein.•2-Hydroxypropyl-b-cyclodextrin decelerates stage of structural reorganization of irradiated enzyme and nucleation stage.